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- PDB-2req: METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CON... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2req | ||||||
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Title | METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE | ||||||
![]() | (METHYLMALONYL-COA MUTASE) x 2 | ||||||
![]() | ISOMERASE / MUTASE / INTRAMOLECULAR TRANSFERASE | ||||||
Function / homology | ![]() lactate fermentation to propionate and acetate / propionate metabolic process, methylmalonyl pathway / methylmalonyl-CoA mutase / methylmalonyl-CoA mutase activity / cobalamin binding / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Evans, P.R. / Mancia, F. | ||||||
![]() | ![]() Title: Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism. Authors: Mancia, F. / Evans, P.R. #1: ![]() Title: How Coenzyme B12 Radicals are Generated: The Crystal Structure of Methylmalonyl-Coenzyme a Mutase at 2 A Resolution Authors: Mancia, F. / Keep, N.H. / Nakagawa, A. / Leadlay, P.F. / Mcsweeney, S. / Rasmussen, B. / Bosecke, P. / Diat, O. / Evans, P.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 540.1 KB | Display | ![]() |
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PDB format | ![]() | 430.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.7 MB | Display | ![]() |
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Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 107.2 KB | Display | |
Data in CIF | ![]() | 144.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3reqC ![]() 4reqC ![]() 1reqS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.320376, 0.104528, 0.941506), Vector: Details | THE CRYSTAL ASYMMETRIC UNIT CONSISTS OF TWO HETERODIMERIC MOLECULES, EACH WITH AN ACTIVE ALPHA CHAIN (CHAINS A AND C), AND AN INACTIVE BETA CHAIN (CHAINS B AND D). EACH ALPHA CHAIN CONTAINS A COBALAMIN, MODELLED AS A 5-COORDINATE CO(II) SPECIES, AND A COENZYME A MOLECULE APPROXIMATELY IN THE SUBSTRATE BINDING SITE, BUT WITH THE PANTOTHEINE SIDE CHAIN DISORDERED. THE WATERS ARE ASSOCIATED WITH PROTEIN CHAINS AS FOLLOWS: PROTEIN CHAINS WATERS A AND B X C AND D Y | |
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Components
#1: Protein | Mass: 80137.852 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: CHAINS A AND C INCLUDE COENZYME B12, AND COA. B12 IS PRESENT LARGELY AS REDUCED COB(II)ALAMIN, OR B12R. COA IS ONLY PARTLY ORDERED AND IS NOT BOUND CORRECTLY IN THE TRUE SUBSTRATE SITE Source: (gene. exp.) ![]() Species: Propionibacterium freudenreichii / Strain: NCIB 9885 Description: THE 2 GENES MUTA (BETA CHAIN) AND MUTB (ALPHA CHAIN) ARE COEXPRESSED FROM THE SAME PLASMID Gene: MUTA, MUTB / Plasmid: PMEX2 / Cellular location (production host): CYTOPLASM / Gene (production host): MUTA, MUTB / Production host: K38 PGP1-2 / References: UniProt: P11653, methylmalonyl-CoA mutase #2: Protein | Mass: 69430.188 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: CHAINS A AND C INCLUDE COENZYME B12, AND COA. B12 IS PRESENT LARGELY AS REDUCED COB(II)ALAMIN, OR B12R. COA IS ONLY PARTLY ORDERED AND IS NOT BOUND CORRECTLY IN THE TRUE SUBSTRATE SITE Source: (gene. exp.) ![]() Species: Propionibacterium freudenreichii / Strain: NCIB 9885 Description: THE 2 GENES MUTA (BETA CHAIN) AND MUTB (ALPHA CHAIN) ARE COEXPRESSED FROM THE SAME PLASMID Gene: MUTA, MUTB / Plasmid: PMEX2 / Cellular location (production host): CYTOPLASM / Gene (production host): MUTA, MUTB / Production host: K38 PGP1-2 / References: UniProt: P11652, methylmalonyl-CoA mutase #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | THIS STRUCTURE IS IN THE OPEN SUBSTRATE-FREE CONFORMATION, WITH THE SUBSTRATE ANALOGUE COA BOUND IN ...THIS STRUCTURE IS IN THE OPEN SUBSTRATE-FREE CONFORMATI | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56 % / Description: DATA COLLECTED AT ELETTRA, TRIESTE, ITALY | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion / pH: 7.5 Details: PROTEIN SOLUTION: 20 MG/ML PROTEIN, 1MM ADENOSYLCOBALAMIN, 2MM COA, 1MM DTT, TRIS -HCL PH 7.5. RESERVOIR SOLUTION: 17.5% (W/V) PEG4000, 20% GLYCEROL (V/V), 100MM TRIS-HCL PH 7.5. EQUAL ...Details: PROTEIN SOLUTION: 20 MG/ML PROTEIN, 1MM ADENOSYLCOBALAMIN, 2MM COA, 1MM DTT, TRIS -HCL PH 7.5. RESERVOIR SOLUTION: 17.5% (W/V) PEG4000, 20% GLYCEROL (V/V), 100MM TRIS-HCL PH 7.5. EQUAL VOLUMES OF PROTEIN SOLUTION WERE MIXED AND EQUILIBRATED BY VAPOR DIFFUSION., vapor diffusion | |||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 23 ℃ / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 180 mm plate / Detector: IMAGE PLATE / Date: Jul 1, 1995 / Details: TOROIDAL MIRROR, SI MONOCHROMATOR |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.24 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 113512 / % possible obs: 99.8 % / Observed criterion σ(I): 3.5 / Redundancy: 4.8 % / Biso Wilson estimate: 55 Å2 / Rmerge(I) obs: 0.092 / Net I/σ(I): 6 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.338 / Mean I/σ(I) obs: 2.1 / % possible all: 99.7 |
Reflection shell | *PLUS Highest resolution: 2.5 Å / % possible obs: 99.7 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1REQ Resolution: 2.5→20 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 47 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 113303 / Rfactor all: 0.259 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |